O86309 (NAT_MYCSM) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Arylamine N-acetyltransferase
EC=2.3.1.5

Gene names

Name:

nat

Organism

Mycobacterium smegmatis

Taxonomic identifier

1772 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium

Protein attributes

Sequence length	275 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Could have a role in acetylating, and hence inactivating, the antitubercular drug isoniazid.
Catalytic activity	Acetyl-CoA + an arylamine = CoA + an N-acetylarylamine.
Subunit structure	Homodimer. Ref.2
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the arylamine N-acetyltransferase family.
Sequence caution	The sequence CAA07100.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Acyltransferase Transferase
Technical term	3D-structure
Gene Ontology (GO)
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	arylamine N-acetyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 275

275

Arylamine N-acetyltransferase

PRO_0000107918

Sites

Active site

70

1

Acyl-thioester intermediate

Active site

110

1

Active site

127

1

Experimental info

Mutagenesis

70

1

C → A, S or Q: Loss of activity. Ref.3

Mutagenesis

110

1

H → A, R or W: Loss of activity. Ref.3

Mutagenesis

127

1

D → A, N or W: Loss of activity. Ref.3

Secondary structure

1

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275

Helix Strand Turn

Details...

Helix

5 – 11

7

Helix

22 – 35

14

Helix

41 – 44

4

Helix

54 – 61

8

Turn

62 – 64

3

Helix

70 – 84

15

Beta strand

87 – 95

9

Beta strand

108 – 116

9

Beta strand

120 – 122

3

Beta strand

124 – 126

3

Beta strand

139 – 141

3

Beta strand

143 – 147

5

Beta strand

150 – 152

3

Beta strand

154 – 159

6

Beta strand

162 – 169

8

Beta strand

172 – 179

8

Helix

186 – 198

13

Helix

203 – 206

4

Beta strand

209 – 213

5

Beta strand

215 – 222

8

Beta strand

225 – 230

6

Beta strand

233 – 241

9

Helix

242 – 251

10

Helix

257 – 260

4

Helix

265 – 271

7

Turn

272 – 274

3

Sequences

	Sequence		Length	Mass (Da)
	O86309 [UniParc]. Last modified December 1, 2000. Version 3. Checksum: C35800574905D3B9	FASTA	275	30,174
	10 20 30 40 50 60 MAMDLGGYLT RIGLDGRPRP DLGTLHAIVA AHNRSIPFEN LDPLLGIPVA DLSAEALFAK 70 80 90 100 110 120 LVDRRRGGYC YEHNGLLGYV LEELGFEVER LSGRVVWMRA DDAPLPAQTH NVLSVAVPGA 130 140 150 160 170 180 DGRYLVDVGF GGQTLTSPIR LEAGPVQQTR HEPYRLTRHG DDHTLAAQVR GEWQPLYTFT 190 200 210 220 230 240 TEPRPRIDLE VGSWYVSTHP GSHFVTGLTV AVVTDDARYN LRGRNLAVHR SGATEHIRFD 250 260 270 SAAQVLDAIV NRFGIDLGDL AGRDVQARVA EVLDT

References

[1]	"Cloning and characterization of arylamine N-acetyltransferase genes from Mycobacterium smegmatis and Mycobacterium tuberculosis: increased expression results in isoniazid resistance." Payton M.A., Auty R., Delgoda R.T., Everitt M., Sim E. J. Bacteriol. 181:1343-1347(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
[2]	"The structure of arylamine N-acetyltransferase from Mycobacterium smegmatis -- an enzyme which inactivates the anti-tubercular drug, isoniazid." Sandy J., Mushtaq A., Kawamura A., Sinclair J., Sim E., Noble M.E.M. J. Mol. Biol. 318:1071-1083(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), HOMODIMERIZATION.
[3]	"Investigation of the catalytic triad of arylamine N-acetyltransferases: essential residues required for acetyl transfer to arylamines." Sandy J., Mushtaq A., Holton S.J., Schartau P., Noble M.E.M., Sim E. Biochem. J. 390:115-123(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF WILD-TYPE IN COMPLEX WITH ISONIAZID AND OF MUTANT GLN-70, MUTAGENESIS OF CYS-70; HIS-110 AND ASP-127.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AJ006588 Genomic DNA. Translation: CAA07100.2. Different initiation.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GX3	X-ray	1.70	A/B/C/D	1-275	[»]
1W5R	X-ray	1.45	A/B	1-275	[»]
1W6F	X-ray	2.10	A/B/C/D	1-275	[»]

ProteinModelPortal

O86309.

SMR

O86309. Positions 1-275.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR001447. Arylamine_N-AcTrfase.
[Graphical view]

PANTHER

PTHR11786. PTHR11786. 1 hit.

Pfam

PF00797. Acetyltransf_2. 1 hit.
[Graphical view]

PRINTS

PR01543. ANATRNSFRASE.

ProtoNet

Search...

Other

BindingDB

O86309.

ChEMBL

CHEMBL6060.

DrugBank

DB00951. Isoniazid.

EvolutionaryTrace

O86309.

Entry information

Entry name

NAT_MYCSM

Accession

Primary (citable) accession number: O86309

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	December 1, 2000
Last modified:	April 3, 2013
This is version 73 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program